The Presence of a Single N-terminal Histidine Residue Enhances the Fusogenic Properties of a Membranotropic Peptide Derived from Herpes Simplex Virus Type 1 Glycoprotein H

Galdiero, Stefania; Falanga, Annarita; Vitiello, Mariateresa; Raiola, Luca; Russo, Luca; Pedone, Carlo; Isernia, Carla; Galdiero, Massimiliano

doi:10.1074/jbc.m110.114819

Cited by 51 publications

(88 citation statements)

References 73 publications

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“…10 Briefly, peptides were obtained using a Wang (0.58 mmol g -1 ) resin by consecutive deprotection (30% piperidine) and coupling (2 equivalents of amino acid, 2 equivalents of 1-Hydroxybenzotriazole (HOBT)/3-[Bis(dimethylamino)methyliumyl]-3H-benzotriazol-1-oxide hexafluorophosphate (HBTU) and 4 equivalents of DIPEA) steps. Peptides were fully deprotected and cleaved from the resin with trifluoroacetic acid (TFA)/5% thioanisole/3% ethandithiol/2% anisole as scavengers for 90 min.…”

Section: Peptide Synthesismentioning

confidence: 99%

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Daphnia magna and Xenopus laevis as in vivo models to probe toxicity and uptake of quantum dots functionalized with gH625

Galdiero¹,

Falanga²,

Siciliano³

et al. 2017

IJN

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The use of quantum dots (QDs) for nanomedicine is hampered by their potential toxicologic effects and difficulties with delivery into the cell interior. We accomplished an in vivo study exploiting Daphnia magna and Xenopus laevis to evaluate both toxicity and uptake of QDs coated with the membranotropic peptide gH625 derived from the glycoprotein H of herpes simplex virus and widely used for drug delivery studies. We evaluated and compared the effects of QDs and gH625-QDs on the survival, uptake, induction of several responsive pathways and genotoxicity in D. magna , and we found that QDs coating plays a key role. Moreover, studies on X. laevis embryos allowed to better understand their cell/tissue localization and delivery efficacy. X. laevis embryos raised in Frog Embryo Teratogenesis Assay- Xenopus containing QDs or gH625-QDs showed that both nanoparticles localized in the gills, lung and intestine, but they showed different distributions, indicating that the uptake of gH625-QDs was enhanced; the functionalized QDs had a significantly lower toxic effect on embryos’ survival and phenotypes. We observed that D. magna and X. laevis are useful in vivo models for toxicity and drug delivery studies.

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Section: Peptide Synthesismentioning

confidence: 99%

“…10,11 This peptide has proved to exhibit exceptional vector properties 9 and has been shown to be essentially internalized by a nonendocytic pathway avoiding endosomal entrapment. 7,[12][13][14][15][16][17] In recent studies, it was also shown to be able to cross the blood-brain barrier in vitro and in vivo.…”

Section: Introductionmentioning

confidence: 99%

Daphnia magna and Xenopus laevis as in vivo models to probe toxicity and uptake of quantum dots functionalized with gH625

Galdiero¹,

Falanga²,

Siciliano³

et al. 2017

IJN

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“…13 The peptide was obtained with good yields (30%-40%). Labeling was performed on resin-bound peptides as previously reported by Rapaport and Shai.…”

Section: Peptide Synthesismentioning

confidence: 99%

“…10,11 The intrinsic ability of virus-derived peptides to induce membrane perturbation may be useful in the design of delivery vehicles. [12][13][14] The peptide gH625, previously identified as a membraneperturbing domain in glycoprotein H (gH) of herpes simplex virus 1, has been demonstrated to be able to traverse the membrane bilayer. 15 Further, gH625 has been used extensively for vector-mediated strategies that enable passage of a large variety of small molecules as well as proteins across cell membranes in vitro.…”

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confidence: 99%

Peptide gH625 enters into neuron and astrocyte cell lines and crosses the blood–brain barrier in rats

Valiante¹,

Falanga²,

Cigliano³

et al. 2015

IJN

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Peptide gH625, derived from glycoprotein H of herpes simplex virus type 1, can enter cells efficiently and deliver a cargo. Nanoparticles armed with gH625 are able to cross an in vitro model of the blood–brain barrier (BBB). In the present study, in vitro experiments were performed to investigate whether gH625 can enter and accumulate in neuron and astrocyte cell lines. The ability of gH625 to cross the BBB in vivo was also evaluated. gH625 was administered in vivo to rats and its presence in the liver and in the brain was detected. Within 3.5 hours of intravenous administration, gH625 can be found beyond the BBB in proximity to cell neurites. gH625 has no toxic effects in vivo, since it does not affect the maximal oxidative capacity of the brain or the mitochondrial respiration rate. Our data suggest that gH625, with its ability to cross the BBB, represents a novel nanocarrier system for drug delivery to the central nervous system. These results open up new possibilities for direct delivery of drugs into patients in the field of theranostics and might address the treatment of several human diseases.

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“…12 Viral-derived peptides, in particular those derived from viral entry proteins, may be useful as delivery vehicles due to their intrinsic properties of inducing membrane perturbation. [13][14][15] Delivery across cellular membranes involves several mechanisms such as direct transfer through cell surface membrane by lipid membrane fusion or transient permeabilization of the cell membrane; or after endocytosis, transfer across vesicular membranes by lipid disruption, pore formation, or fusion.…”

Section: Introductionmentioning

confidence: 99%

gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins

Smaldone¹,

Falanga²,

Capasso³

et al. 2013

IJN

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A genetically modified recombinant gH625-c-prune was prepared through conjugation of c-prune with gH625, a peptide encompassing 625-644 residues of the glycoprotein H of herpes simplex virus 1, which has been proved to possess the ability to carry cargo molecules across cell membranes. C-prune is the C-terminal domain of h-prune, overexpressed in breast, colorectal, and gastric cancers, interacting with multiple partners, and representing an ideal target for inhibition of cancer development. Its C-terminal domain results in an intrinsically disordered domain (IDD), and the peculiar properties of gH625 render it an optimal candidate to act as a carrier for this net negatively charged molecule by comparison with the positively charged TAT. A characterization of the recombinant gH625-c-prune fusion protein was conducted by biochemical, cellular biology and confocal microscopy means in comparison with TAT-c-prune. The results showed that the gH625-c-prune exhibited the ability to cross biomembranes, opening a new scenario on the use of gH625 as a novel multifunctional carrier.

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The Presence of a Single N-terminal Histidine Residue Enhances the Fusogenic Properties of a Membranotropic Peptide Derived from Herpes Simplex Virus Type 1 Glycoprotein H

Cited by 51 publications

References 73 publications

<em>Daphnia magna</em> and<em> Xenopus laevis</em> as in vivo models to probe toxicity and uptake of quantum dots functionalized with gH625

<em>Daphnia magna</em> and<em> Xenopus laevis</em> as in vivo models to probe toxicity and uptake of quantum dots functionalized with gH625

Peptide gH625 enters into neuron and astrocyte cell lines and crosses the blood–brain barrier in rats

gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins

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The Presence of a Single N-terminal Histidine Residue Enhances the Fusogenic Properties of a Membranotropic Peptide Derived from Herpes Simplex Virus Type 1 Glycoprotein H

Cited by 51 publications

References 73 publications

<em>Daphnia magna</em> and<em> Xenopus laevis</em> as in vivo models to probe toxicity and uptake of quantum dots functionalized with gH625

<em>Daphnia magna</em> and<em> Xenopus laevis</em> as in vivo models to probe toxicity and uptake of quantum dots functionalized with gH625

Peptide gH625 enters into neuron and astrocyte cell lines and crosses the blood&ndash;brain barrier in&nbsp;rats

gH625 is a viral derived peptide for effective delivery of intrinsically disordered proteins

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Peptide gH625 enters into neuron and astrocyte cell lines and crosses the blood–brain barrier in rats